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* Department of Medicine, UCLA School of Medicine, and
|| Molecular Biology Institute, UCLA, Los Angeles, California;
A. A. Ukhtomsky Physiology Research Institute, St. Petersburg State University, and
Institute of Experimental Medicine, St. Petersburg, Russia; and
Department of Pathology and Laboratory Medicine, MCP Hahnemann School of Medicine, Philadelphia, Pennsylvania
Correspondence: Robert I. Lehrer, M.D., Department of Medicine, UCLA Center for the Health Sciences, Los Angeles, CA 90095-1690. E-mail: rlehrer{at}mednet.ucla.edu
We purified two new minidefensins (RTD-2 and RTD-3) from the bone
marrow of rhesus monkeys. Both were circular octadecapeptides that
contained three intramolecular disulfide bonds and were homologous to
RTD-1, a circular (
) defensin previously described by Tang et al.
(Science, 286, 498–502, 1999). However, whereas the 18
residues of RTD-1 represent spliced nonapeptide fragments derived from
two different demidefensin precursors, RTD-2 and -3 comprise tandem
nonapeptide repeats derived from only one of the RTD-1 precursors.
Thus, circular minidefensins are products of a novel posttranslational
system that generates effector molecule diversity without commensurate
genome expansion. A system wherein two demidefensin genes can produce
three circular minidefensins might allow n such genes to
produce (n/2)(n+1) peptides.
Key Words: antimicrobial • peptides • defensins • innate immunity • RTD
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